Abstract
A new method for the synthesis of β-N-(γ-l(+)-glutamyl)phenylhydrazine is presented. This compound was prepared from l-glutamine and phenylhydrazine through a transpeptidation reaction of Escherichia coli γ-glutamyltranspeptidase although phenylhydrazine has been reported to be an inhibitor of the enzyme. The optimum reaction conditions were 60 mM l-glutamine, 300 mM phenylhydrazine, 40 U γ-glutamyltranspeptidase/ml, and pH 9 in approx. 800 ml. After 6 h at 37 °C, the product was obtained with a conversion rate of 93 % (mol/mol). γ-Glutamyltranspeptidase was reversibly inhibited only when phenylhydrazine was above 300 mM.
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This work was supported by Jiangsu Planned Projects for Postdoctoral Research Funds (1101005C) and the Open Fund of State Key Laboratory of Pharmaceutical Biotechnology of Nanjing University, China.
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Zhang, H., Zhan, Y., Chang, J. et al. Enzymatic synthesis of β-N-(γ-l(+)-glutamyl)phenylhydrazine with Escherichia coli γ-glutamyltranspeptidase. Biotechnol Lett 34, 1931–1935 (2012). https://doi.org/10.1007/s10529-012-1000-x
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DOI: https://doi.org/10.1007/s10529-012-1000-x